9RLJ: LolCDE with bound ATPgammaS

Name: PDB 9RLJ: LolCDE with bound ATPgammaS
Published: 2026-01-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: protein transport

LolCDE with bound ATPgammaS. Determined by electron microscopy at 2.9 Å resolution. Released 21 Jan 2026.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Escherichia coli K-12
Chains: 4
Atoms: 9,775
Mol. weight: 142.39 kDa
Ligands: MG, AGS
Released: 21 Jan 2026

Explore 9RLJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9RLJ contains 51 α-helices and 56 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain C: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	21-27	7
α-helix	29-55	27
α-helix	56-60	5
β-strand	66-69	4	1
β-strand	75	1	2
α-helix	76	1
α-helix	82-84	3
β-strand	90-96	7	1
β-strand	98-104	7	3
β-strand	109-117	9	3
α-helix	126-128	3
β-strand	129-130	2	3
α-helix	134-136	3
β-strand	143-147	5	3
α-helix	148-154	7
β-strand	161	1	3
β-strand	163-165	3	3
β-strand	170-171	2	4
β-strand	178-179	2	4
β-strand	185-190	6	3
α-helix	195-197	3
β-strand	200-204	5	3
α-helix	205-211	7
β-strand	219	1	2
β-strand	221-226	6	1
α-helix	234-237	4
α-helix	240-241	2
β-strand	245-248	4	1
α-helix	255-292	38
α-helix	296-303	8
α-helix	307-346	40
α-helix	362-379	18
α-helix	381-388	8
α-helix	392-396	5

Chain D: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	8
β-strand	11-16	6	9
β-strand	21-28	8	9
β-strand	31-33	3	8
β-strand	37-42	6	10
α-helix	48-55	8
β-strand	65-68	4	8
β-strand	71-72	2	8
α-helix	78-87	10
β-strand	89-92	4	10
α-helix	104-115	12
α-helix	119-133	15
α-helix	148-160	13
β-strand	166-170	5	10
α-helix	178-194	17
β-strand	198-203	6	10
α-helix	206-209	4
β-strand	216-219	4	10
β-strand	222-223	2	10

Chain E: 17 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	5-14	10
α-helix	25-54	30
α-helix	55-59	5
β-strand	66-70	5	5
α-helix	83-86	4
β-strand	91-93	3	6
β-strand	96-100	5	5
β-strand	103	1	7
β-strand	112	1	7
β-strand	115-118	4	5
α-helix	129-132	4
β-strand	133	1	5
β-strand	147-151	5	5
α-helix	152-158	7
β-strand	166-170	5	7
β-strand	183-187	5	7
β-strand	188-193	6	5
α-helix	198-201	4
β-strand	204-205	2	5
β-strand	207	1	5
α-helix	208-213	6
β-strand	223-225	3	5
β-strand	227-228	2	6
α-helix	231-233	3
α-helix	234-244	11
β-strand	249-253	5	5
α-helix	254-257	4
α-helix	262-296	35
α-helix	299-307	9
α-helix	312-320	9
α-helix	326-343	18
α-helix	345-356	12
α-helix	377-402	26

Chain F: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	11
β-strand	11-15	5	12
β-strand	22-28	7	12
β-strand	31-33	3	11
β-strand	37-41	5	13
α-helix	48-55	8
β-strand	65-68	4	11
β-strand	72	1	11
α-helix	78-87	10
β-strand	89-92	4	13
α-helix	104-115	12
α-helix	119-133	15
α-helix	136-138	3
α-helix	148-160	13
β-strand	166-170	5	13
α-helix	178-194	17
β-strand	198-203	6	13
α-helix	206-209	4
β-strand	214-219	6	13
β-strand	222-224	3	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lipoprotein-releasing system transmembrane protein LolC	C	protein	399	Escherichia coli K-12	P0ADC3 (AlphaFold model)
Lipoprotein-releasing system transmembrane protein LolE	E	protein	414	Escherichia coli K-12	P75958 (AlphaFold model)
Lipoprotein-releasing system ATP-binding protein LolD	D, F	protein	240	Escherichia coli K-12	P75957 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>9RLJ_1 Lipoprotein-releasing system transmembrane protein LolC (chains C)
MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL
GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA
QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS
QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL
PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL
QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI
EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE

Sequence of entity 2 (E), FASTA

>9RLJ_2 Lipoprotein-releasing system transmembrane protein LolE (chains E)
MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL
AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP
QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM
QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRD
AGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSG
DIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQF
LSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ

Sequence of entity 3 (D, F), FASTA

>9RLJ_3 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F)
MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT
PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA
EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN
ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAEGSHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	2

Primary citation

Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport. Szewczyk, P., Greene, N.P., Symmons, M.F. et al. Proc Natl Acad Sci U S A (2026) 123:e2520579123-e2520579123. DOI 10.1073/pnas.2520579123 · PubMed

Other PDB entries of the same protein (UniProt P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NAA 1.88 Å, Lipoprotein-releasing system transmembrane protein LolC
6F3Z 2.0 Å, Complex of E. coli LolA and periplasmic domain of LolC
6F49 2.02 Å, Periplasmic domain of LolC lacking the Hook.
9RLC 2.8 Å, LolCDE complex with Lpp lipoprotein
9XRO 2.88 Å, LolCDE in complex with SMT-738_3
9RLD 3.0 Å, LolCDE complex with Lpp lipoprotein
9RLG 3.09 Å, LolCDE complex with LolB lipoprotein
9RLF 3.17 Å, LolCDE complex with Pal lipoprotein
9RLE 3.18 Å, LolCDE complex with Pal lipoprotein
9RLH 3.19 Å, LolCDE complex with del 9-15 LolB lipoprotein
7ARJ 3.2 Å, LolCDE in complex with lipoprotein and AMPPNP complex undimerized form
7ARL 3.2 Å, LolCDE in complex with lipoprotein and ADP

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